Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils

Title: Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils

Volume: 12 Issue: 1

Author(s): Victoria L. Sedman, Stephanie Allen, Weng C. Chan, Martyn C. Davies, Clive J. Roberts, Saul J.B. Tendler and Philip M. Williams

Affiliation:

Keywords: protein aggregation, designability, protein folding, protein design, amyloid

Abstract: Here we present atomic force microscopy images of the fibrils formed by human amylin(20-29). This peptide is a fragment of the polypeptide amylin, the major proteinaceous component of amyloid deposits found in cases of type-II diabetes mellitus. Our results demonstrate that the amylin(20-29) peptide fragment forms amyloid-like fibrils that display polymorphic structures. Twisting along the axis of fibrils was often observed in fibrils aged for 6 hours but disappeared in mature fibrils aged for longer time periods.

Cite this article as:

Sedman L. Victoria, Allen Stephanie, Chan C. Weng, Davies C. Martyn, Roberts J. Clive, Tendler J.B. Saul and Williams M. Philip, Atomic Force Microscopy Study of Human Amylin (20-29) Fibrils, Protein & Peptide Letters 2005; 12 (1) . https://dx.doi.org/10.2174/0929866053406129